Production of recombinant proteins in hosts is a common process used both by researchers and commercial entities for the manufacture of a large variety of proteins. In many instances, the protein is not produced efficiently in particular host, so these proteins must be produced through a different expression system. Unfortunately, conventional methods of determining the efficiency of protein expression in a particular host require a number of time-consuming steps. One method involves destroying the host, isolating proteins therefrom, and resolving the isolated proteins on a gel to detect the presence of product bands at a particular molecular weight. Another method involves destroying the host, and performing a Western blot for the protein of interest. In addition to being time-consuming, both methods involve either knowledge of the size of the protein of interest or an antibody that specifically recognizes the expressed product. Further, the researcher does not know about failed expression until all the steps are performed. The ability to monitor protein translation directly in hosts, particularly in real-time, is limited.
One method of monitoring protein expression in real-time in hosts is to fuse the protein of interest directly to a fluorescent protein. Protein translation is measured through detection of fluorescence in the host. However, this method is limited in that fusion of the proteins can affect activity of both the protein of interest and the fluorescent protein and makes purification and isolation of the protein of interest difficult.
Therefore, there remains a long-felt and unmet need for a system and method for quickly and reliably determining whether any given host is capable of expressing the gene product of any given gene.